Abstract
Calculation of the free energy profile for hydrolysis of phosphohistidine using ONIOM methodology indicates a much tighter transition state in the enzyme active site compared to that in explicit water and elucidates the role of active site residues in catalysis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acid Phosphatase
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Biocatalysis
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Catalytic Domain
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Histidine / analogs & derivatives*
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Histidine / chemistry
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Histidine / metabolism
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Hydrolysis
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Protein Tyrosine Phosphatases / metabolism*
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Water / chemistry*
Substances
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Water
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Histidine
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Acid Phosphatase
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prostatic acid phosphatase
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Protein Tyrosine Phosphatases
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phosphohistidine